| Literature DB >> 10766029 |
J J Calvete1, F H Costa, S Saker-Sampaio, M P Murciano, C S Nagano, B S Cavada, T B Grangeiro, M V Ramos, C Bloch, S B Silveira, B T Freitas, A H Sampaio.
Abstract
The primary structure of a lectin isolated from the red alga Bryothamnion triquetrum was established by combination of Edman degradation of sets of overlapping peptides and mass spectrometry. It contains 91 amino acids and two disulphide bonds. The primary structure of the B. triquetrum lectin does not show amino acid sequence similarity with known plant and animal lectin structures. Hence, this protein may be the paradigm of a novel lectin family.Entities:
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Year: 2000 PMID: 10766029 DOI: 10.1007/PL00000696
Source DB: PubMed Journal: Cell Mol Life Sci ISSN: 1420-682X Impact factor: 9.261